ID   EST2_PSEFL              Reviewed;         218 AA.
AC   Q53547;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Carboxylesterase 2;
DE            EC=3.1.1.1;
DE   AltName: Full=Esterase II;
GN   Name=estB;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1368750; DOI=10.1271/bbb1961.55.2839;
RA   Hong K.H., Jang W.H., Choi K.D., Yoo O.J.;
RT   "Characterization of Pseudomonas fluorescens carboxylesterase: cloning and
RT   expression of the esterase gene in Escherichia coli.";
RL   Agric. Biol. Chem. 55:2839-2845(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, AND ACTIVE SITES.
RX   PubMed=9438866; DOI=10.1016/s0969-2126(97)00306-7;
RA   Kim K.K., Song H.K., Shin D.H., Hwang K.Y., Choe S., Yoo O.J., Suh S.W.;
RT   "Crystal structure of carboxylesterase from Pseudomonas fluorescens, an
RT   alpha/beta hydrolase with broad substrate specificity.";
RL   Structure 5:1571-1584(1997).
CC   -!- FUNCTION: Hydrolyzes carboxylic ester bonds with relatively broad
CC       substrate specificity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9438866}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
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DR   EMBL; S79600; AAC60403.1; -; Genomic_DNA.
DR   PIR; JU0277; JU0277.
DR   RefSeq; WP_065907026.1; NZ_CP031450.1.
DR   PDB; 1AUO; X-ray; 1.80 A; A/B=1-218.
DR   PDB; 1AUR; X-ray; 2.50 A; A/B=1-218.
DR   PDBsum; 1AUO; -.
DR   PDBsum; 1AUR; -.
DR   AlphaFoldDB; Q53547; -.
DR   SMR; Q53547; -.
DR   STRING; 690597.JH730920_gene1178; -.
DR   DrugBank; DB03297; Benzylsulfonic acid.
DR   ESTHER; psefl-cxest; LYsophospholipase_carboxylesterase.
DR   eggNOG; COG0400; Bacteria.
DR   EvolutionaryTrace; Q53547; -.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Serine esterase.
FT   CHAIN           1..218
FT                   /note="Carboxylesterase 2"
FT                   /id="PRO_0000102275"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:9438866"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:9438866"
FT   ACT_SITE        199
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:9438866"
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          14..20
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   TURN            27..30
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           31..38
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           81..100
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           173..184
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          190..196
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:1AUO"
FT   HELIX           203..217
FT                   /evidence="ECO:0007829|PDB:1AUO"
SQ   SEQUENCE   218 AA;  23880 MW;  6F1D4557410E4CB4 CRC64;
     MTEPLILQPA KPADACVIWL HGLGADRYDF MPVAEALQES LLTTRFVLPQ APTRPVTING
     GYEMPSWYDI KAMSPARSIS LEELEVSAKM VTDLIEAQKR TGIDASRIFL AGFSQGGAVV
     FHTAFINWQG PLGGVIALST YAPTFGDELE LSASQQRIPA LCLHGQYDDV VQNAMGRSAF
     EHLKSRGVTV TWQEYPMGHE VLPQEIHDIG AWLAARLG